Structure of PDB 1lld Chain A

Receptor sequence
>1lldA (length=313) Species: 1679 (Bifidobacterium longum subsp. longum) [Search protein sequence]
PTKLAVIGAGAVGSTLAFAAAQRGIAREIVLEDIAKERVEAEVLDMQHGS
SFYPTVSIDGSDDPEICRDADMVVITAGPRQKPGQSRLELVGATVNILKA
IMPNLVKVAPNAIYMLITNPVDIATHVAQKLTGLPENQIFGSGTNLDSAR
LRFLIAQQTGVNVKNVHAYIAGEHGDSEVPLWESATIGGVPMSDWTPLPG
HDPLDADKREEIHQEVKNAAYKIINGKGATNYAIGMSGVDIIEAVLHDTN
RILPVSSMLKDFHGISDICMSVPTLLNRQGVNNTINTPVSDKELAALKRS
AETLKETAAQFGF
3D structure
PDB1lld Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R93 D153 R156 H180
Catalytic site (residue number reindexed from 1) R87 D147 R150 H174
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD A G16 A17 V18 D39 I40 R44 T82 A83 I107 N125 H180 I230 I240 G10 A11 V12 D33 I34 R38 T76 A77 I101 N119 H174 I224 I234
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0006096 glycolytic process
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lld, PDBe:1lld, PDBj:1lld
PDBsum1lld
PubMed8450537
UniProtE8ME30|LDH2_BIFL2 L-lactate dehydrogenase 2 (Gene Name=ldh2)

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